抗人 SULT1A1 抗体对
01AB01365
Sulfotransferase family 1A member 1 (SULT1A1) is a cytosolic phase II enzyme that catalyzes the transfer of a sulfate group from the cofactor 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to hydroxyl and amine groups of various substrates, including hormones, neurotransmitters, drugs, and xenobiotics. Structurally, SULT1A1 features a single α/β domain with a central five-stranded parallel β-sheet and a dynamic active-site cap that regulates substrate access. Key loops (L1, L2, L3) form a gating mechanism controlling substrate binding, with phenylalanine residues (F81, F84) acting as a molecular clamp to enhance substrate affinity and catalysis. The enzyme exhibits tissue-dependent substrate specificity influenced by PAPS occupancy and harbors two allosteric sites that modulate activity. Functionally, SULT1A1 plays a major role in hepatic detoxification and metabolism. Variations in SULT1A1 activity and expression are linked to altered drug metabolism and susceptibility to cancers, such as breast and lung cancer, and influence responses to environmental toxins and carcinogens.
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技术参数
- 靶点基因名
- SULT1A1
- 基因别名
- STP; STP1
- 蛋白别名
- sulfotransferase family 1A member 1; SULT1A1
- UniProt
- P50225
- 物种
- Human
产品详情
- 靶点名称
- SULT1A1
- 蛋白名称
- sulfotransferase family 1A member 1
- 蛋白别名
- Sulfotransferase 1A1; ST1A1; Aryl sulfotransferase 1; HAST1/HAST2; Phenol sulfotransferase 1; Phenol-sulfating phenol sulfotransferase 1; P-PST 1; ST1A3; Thermostable phenol sulfotransferase; Ts-PST
- 靶点基因名
- SULT1A1
- 基因别名
- STP; STP1
- UniProt
- P50225
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Sulfotransferase family 1A member 1 (SULT1A1) is a cytosolic phase II enzyme that catalyzes the transfer of a sulfate group from the cofactor 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to hydroxyl and amine groups of various substrates, including hormones, neurotransmitters, drugs, and xenobiotics. Structurally, SULT1A1 features a single α/β domain with a central five-stranded parallel β-sheet and a dynamic active-site cap that regulates substrate access. Key loops (L1, L2, L3) form a gating mechanism controlling substrate binding, with phenylalanine residues (F81, F84) acting as a molecular clamp to enhance substrate affinity and catalysis. The enzyme exhibits tissue-dependent substrate specificity influenced by PAPS occupancy and harbors two allosteric sites that modulate activity. Functionally, SULT1A1 plays a major role in hepatic detoxification and metabolism. Variations in SULT1A1 activity and expression are linked to altered drug metabolism and susceptibility to cancers, such as breast and lung cancer, and influence responses to environmental toxins and carcinogens.